Basir Ahmad

2.3k total citations
67 papers, 2.0k citations indexed

About

Basir Ahmad is a scholar working on Molecular Biology, Physiology and Oncology. According to data from OpenAlex, Basir Ahmad has authored 67 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 52 papers in Molecular Biology, 15 papers in Physiology and 12 papers in Oncology. Recurrent topics in Basir Ahmad's work include Protein Interaction Studies and Fluorescence Analysis (32 papers), Protein Structure and Dynamics (20 papers) and Alzheimer's disease research and treatments (14 papers). Basir Ahmad is often cited by papers focused on Protein Interaction Studies and Fluorescence Analysis (32 papers), Protein Structure and Dynamics (20 papers) and Alzheimer's disease research and treatments (14 papers). Basir Ahmad collaborates with scholars based in India, United States and Saudi Arabia. Basir Ahmad's co-authors include Rizwan Hasan Khan, Lisa J. Lapidus, Suphiya Parveen, Priyankar Sen, Raghuvir R. S. Pissurlenkar, Sadaf Fatima, Soghra Khatun Haq, Gulam Rabbani, Yujie Chen and Nida Zaidi and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and PLoS ONE.

In The Last Decade

Basir Ahmad

64 papers receiving 2.0k citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Basir Ahmad India 26 1.5k 421 410 298 293 67 2.0k
Masihuz Zaman India 23 1.3k 0.8× 365 0.9× 533 1.3× 205 0.7× 170 0.6× 52 1.7k
Mohammad Khursheed Siddiqi India 25 1.3k 0.9× 438 1.0× 730 1.8× 270 0.9× 195 0.7× 55 1.9k
Sumit Kumar Chaturvedi India 26 1.6k 1.1× 497 1.2× 700 1.7× 364 1.2× 253 0.9× 59 2.3k
Ana M. Damas Portugal 30 1.5k 1.0× 221 0.5× 613 1.5× 212 0.7× 315 1.1× 85 2.3k
Parvez Alam India 37 2.2k 1.5× 767 1.8× 1.0k 2.4× 496 1.7× 401 1.4× 63 3.4k
Nida Zaidi India 21 1.4k 0.9× 566 1.3× 272 0.7× 262 0.9× 194 0.7× 33 1.7k
Carmelo La Rosa Italy 29 1.8k 1.2× 213 0.5× 1.3k 3.2× 171 0.6× 304 1.0× 96 2.6k
Ali S. Abdelhameed Saudi Arabia 29 1.5k 1.0× 660 1.6× 274 0.7× 402 1.3× 160 0.5× 153 2.5k
Li Zhou China 27 1.8k 1.2× 269 0.6× 172 0.4× 88 0.3× 365 1.2× 113 3.0k
Mohd Ishtikhar India 20 880 0.6× 327 0.8× 181 0.4× 270 0.9× 130 0.4× 32 1.2k

Countries citing papers authored by Basir Ahmad

Since Specialization
Citations

This map shows the geographic impact of Basir Ahmad's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Basir Ahmad with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Basir Ahmad more than expected).

Fields of papers citing papers by Basir Ahmad

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Basir Ahmad. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Basir Ahmad. The network helps show where Basir Ahmad may publish in the future.

Co-authorship network of co-authors of Basir Ahmad

This figure shows the co-authorship network connecting the top 25 collaborators of Basir Ahmad. A scholar is included among the top collaborators of Basir Ahmad based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Basir Ahmad. Basir Ahmad is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Parvez, Suhel, et al.. (2025). Conformational constraints and ligand interactions are key determinants of the distinct aggregation pathways observed in human serum albumin. International Journal of Biological Macromolecules. 334(Pt 1). 148952–148952.
2.
Ahmad, Basir, et al.. (2025). Isolation and Identification of Rhizospheric Bacteria from the Juniper Forest of Ziarat, Balochistan. Sarhad Journal of Agriculture. 41(1).
3.
Parvez, Suhel, et al.. (2024). Plumbagin accelerates serum albumin's amyloid aggregation kinetics and generates fibril polymorphism by inducing non-native β-sheet structures. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1872(5). 141028–141028. 2 indexed citations
4.
Ahmad, Musheer, et al.. (2024). A cobalt coordination complex binds on a unique binding site between domain-I and domain-III of serum albumin. Journal of Molecular Structure. 1322. 140345–140345. 4 indexed citations
5.
Sharma, Rahul, et al.. (2024). Redesigning the kinetics of lysozyme amyloid aggregation by cephalosporin molecules. Journal of Biomolecular Structure and Dynamics. 43(18). 10426–10441. 3 indexed citations
6.
Ahmed, Anwar, Salman Alamery, Anas Shamsi, et al.. (2020). Effect of Antioxidants on Heavy Metals Induced Conformational Alteration of Cytochrome C and Myoglobin. Protein and Peptide Letters. 28(1). 31–42. 3 indexed citations
7.
Rajak, Sangam, Yusuf Hussain, Khushboo Singh, et al.. (2020). Cellular Fibronectin Containing Extra Domain A Causes Insulin Resistance via Toll-like Receptor 4. Scientific Reports. 10(1). 9102–9102. 10 indexed citations
8.
Prakash, Prem, et al.. (2020). Herbalome of Chandraprabha vati, a polyherbal formulation of Ayurveda prevents fibrillation of lysozyme by stabilizing aggregation-prone intermediate state. International Journal of Biological Macromolecules. 148. 102–109. 7 indexed citations
9.
Ahmad, Basir, et al.. (2017). Unfolding of CPR3 Gets Initiated at the Active Site and Proceeds via Two Intermediates. Biophysical Journal. 112(4). 605–619. 5 indexed citations
10.
Pissurlenkar, Raghuvir R. S., et al.. (2016). Physical basis for the ofloxacin-induced acceleration of lysozyme aggregation and polymorphism in amyloid fibrils. Archives of Biochemistry and Biophysics. 592. 10–19. 31 indexed citations
11.
Ahmad, Basir, et al.. (2016). A comparative study of fibrillation kinetics of two homologous proteins under identical solution condition. Biochimie. 132. 75–84. 42 indexed citations
12.
Agarwal, Neeraj, et al.. (2015). Effects of 2-amino-8-hydroxyquinoline interaction on the conformation of physiological isomers of human serum albumin. European Biophysics Journal. 44(4). 193–205. 21 indexed citations
13.
Ahmad, Basir, et al.. (2013). Aggregation of Alpha-Synuclein is Kinetically Controlled by Intramolecular Diffusion. Biophysical Journal. 104(2). 51a–51a. 2 indexed citations
14.
Ahmad, Basir, Yujie Chen, & Lisa J. Lapidus. (2012). Aggregation of α-synuclein is kinetically controlled by intramolecular diffusion. Proceedings of the National Academy of Sciences. 109(7). 2336–2341. 76 indexed citations
15.
Fatima, Sadaf, Basir Ahmad, & Rizwan Hasan Khan. (2007). Native‐like tertiary structure in the Mucor miehei lipase molten globule state obtained at low pH. IUBMB Life. 59(3). 179–186. 14 indexed citations
16.
Younus, Hina, Saleha Jamal, Basir Ahmad, & M. Saleemuddin. (2006). Investigation of conformational changes induced by binding of pancreatic RNase to anti-RNase IgG derived Fab monomer using optical procedures. Biochemistry (Moscow). 71(2). 218–221. 3 indexed citations
17.
Gull, Nuzhat, Sanjeev Kumar, Basir Ahmad, Rizwan Hasan Khan, & KABIR‐UD‐DIN KABIR‐UD‐DIN. (2006). Influence of urea additives on micellar morphology/protein conformation. Colloids and Surfaces B Biointerfaces. 51(1). 10–15. 25 indexed citations
18.
Ahmad, Basir & Rizwan Hasan Khan. (2006). Studies on the Acid Unfolded and Molten Globule States of Catalytically Active Stem Bromelain: A Comparison with Catalytically Inactive Form. The Journal of Biochemistry. 140(4). 501–508. 21 indexed citations
19.
Ahmad, Basir, et al.. (2005). Guanidine hydrochloride denaturation of human serum albumin originates by local unfolding of some stable loops in domain III. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1750(1). 93–102. 80 indexed citations
20.
Ahmad, Basir, et al.. (2004). Molten globule-like folding intermediate of asialofetuin at acidic pH. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1699(1-2). 191–199. 19 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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